Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6AYM

Crystal structure of Campylobacter jejuni 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0008782molecular_functionadenosylhomocysteine nucleosidase activity
A0008930molecular_functionmethylthioadenosine nucleosidase activity
A0009086biological_processmethionine biosynthetic process
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0009234biological_processmenaquinone biosynthetic process
A0016787molecular_functionhydrolase activity
A0019284biological_processL-methionine salvage from S-adenosylmethionine
A0019509biological_processL-methionine salvage from methylthioadenosine
A0102246molecular_function6-amino-6-deoxyfutalosine hydrolase activity
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0008782molecular_functionadenosylhomocysteine nucleosidase activity
B0008930molecular_functionmethylthioadenosine nucleosidase activity
B0009086biological_processmethionine biosynthetic process
B0009116biological_processnucleoside metabolic process
B0009164biological_processnucleoside catabolic process
B0009234biological_processmenaquinone biosynthetic process
B0016787molecular_functionhydrolase activity
B0019284biological_processL-methionine salvage from S-adenosylmethionine
B0019509biological_processL-methionine salvage from methylthioadenosine
B0102246molecular_function6-amino-6-deoxyfutalosine hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue EDO A 301
ChainResidue
ASER10
ATHR14
ATYR34
AHOH477
AHOH586

site_idAC2
Number of Residues9
Detailsbinding site for residue EDO A 302
ChainResidue
AILE119
ALEU179
AEDO304
AHOH441
AHOH463
ALEU95
AGLN97
AGLU116
AILE117

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 303
ChainResidue
AASN30
ALYS49
AASN54
AHOH457
BASN115
BLEU179

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 304
ChainResidue
AASN115
AGLU116
AEDO302
AHOH405

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO A 305
ChainResidue
AMET1
AVAL70
AASP122
ALYS124
ALEU125
APRO187
AHOH417

site_idAC6
Number of Residues7
Detailsbinding site for residue EDO A 306
ChainResidue
APRO15
AGLU18
ATHR19
ALYS215
AHOH467
AHOH531
AHOH592

site_idAC7
Number of Residues7
Detailsbinding site for residue EDO B 301
ChainResidue
AASN115
ALEU179
BALA29
BASN30
BLYS49
BASN54
BHOH510

site_idAC8
Number of Residues8
Detailsbinding site for residue EDO B 302
ChainResidue
BGLN97
BGLU116
BILE117
BILE119
BLEU179
BHOH413
BHOH438
BHOH502

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO B 303
ChainResidue
BLYS157
BLYS160
BILE161
BHOH416

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AGLU12
BGLU12

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AASP196
BASP196

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY78
AILE152
AMET172
BGLY78
BILE152
BMET172

220113

PDB entries from 2024-05-22

PDB statisticsPDBj update infoContact PDBjnumon